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Serine/threonine-protein kinase MEC1 (EC 2.7.11.1) (ATR homolog) (DNA-damage checkpoint kinase MEC1) (Mitosis entry checkpoint protein 1)

 ATR_KLULA               Reviewed;        2287 AA.
Q6CT34;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
23-MAY-2018, entry version 92.
RecName: Full=Serine/threonine-protein kinase MEC1;
EC=2.7.11.1;
AltName: Full=ATR homolog;
AltName: Full=DNA-damage checkpoint kinase MEC1;
AltName: Full=Mitosis entry checkpoint protein 1;
Name=MEC1; OrderedLocusNames=KLLA0C15785g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Serine/threonine protein kinase which activates
checkpoint signaling upon genotoxic stresses such as ionizing
radiation (IR), ultraviolet light (UV), or DNA replication
stalling, thereby acting as a DNA damage sensor. Recognizes the
substrate consensus sequence [ST]-Q. Recruited to DNA lesions in
order to initiate the DNA repair by homologous recombination.
Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites
of DNA damage, also involved in the regulation of DNA damage
response mechanism. Required for cell growth and meiotic
recombination (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to
nuclear DNA repair foci in response to DNA double strand breaks.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
{ECO:0000305}.
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EMBL; CR382123; CAH01756.1; -; Genomic_DNA.
RefSeq; XP_452905.1; XM_452905.1.
ProteinModelPortal; Q6CT34; -.
STRING; 284590.XP_452905.1; -.
PRIDE; Q6CT34; -.
EnsemblFungi; CAH01756; CAH01756; KLLA0_C15785g.
GeneID; 2892483; -.
KEGG; kla:KLLA0C15785g; -.
eggNOG; KOG0890; Eukaryota.
eggNOG; COG5032; LUCA.
HOGENOM; HOG000034220; -.
InParanoid; Q6CT34; -.
KO; K02543; -.
OMA; WRRFPEH; -.
OrthoDB; EOG092C00SN; -.
Proteomes; UP000000598; Chromosome C.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IEA:EnsemblFungi.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:EnsemblFungi.
GO; GO:0016572; P:histone phosphorylation; IEA:EnsemblFungi.
GO; GO:2000105; P:positive regulation of DNA-dependent DNA replication; IEA:EnsemblFungi.
GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
Gene3D; 1.10.1070.11; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR003152; FATC_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR012993; UME.
Pfam; PF02260; FATC; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF08064; UME; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SMART; SM00802; UME; 1.
SUPFAM; SSF48371; SSF48371; 3.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
3: Inferred from homology;
ATP-binding; Chromatin regulator; Complete proteome; DNA damage;
DNA repair; Kinase; Meiosis; Nucleotide-binding; Nucleus;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 2287 Serine/threonine-protein kinase MEC1.
/FTId=PRO_0000227711.
DOMAIN 1310 1864 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
DOMAIN 1984 2287 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2255 2287 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
SEQUENCE 2287 AA; 263121 MW; 8A73EB9EE9774995 CRC64;
MDNPRVKYLE ELILALKSAG TVGNGIELDS TLQLDEKNGK LLQTLLKNTQ STNTDEVIFH
KSFQALDLFL RCNQHLFSAN VKEITMIEVI LNNMVSCSLM HWSNMQYIWL INKYVSAWLK
AYSFASTSNL QIWFTEQMVQ YEKLLVTCLR GKLEKPTFHS LLKKIVIVNG WIMRDGLLRN
YSYRRWQSQF QKLMRLLAFV LKSTNEPSVE VASILQLLVR YISLSKESLS IFRFSFDLIQ
TLIKDHHQHI SPTILAKTLL RTLYLCIHDE SKLAEIKNTF ELHEWINTNK NADPLFIRSI
KYVSVKLGFL ESMEEFTFSN KQLHWLHQAI ENPKLRLVSG NVRNCIADSA DIRSFYDKVK
ESLLNTIKDG DTAKLTHSMH SIRQLAIKEK FVNNNLVRSP QVEFNASQNM RLSSLNLVPL
HKSLAFQLLA KHVIKSIPIT DMPEAMLTGV VLILIEVFSR FEPPKLEETS DLIQQSDGYG
CLQVFQRASN SRSRFLRLLS VRLLPYFASL GSKYEDINLK FLIIFLQKPK APYLTETLHM
SWINLIINCN SEYFDDLLLK LIDLFNSSDF AEHTMMAAQL RYLSKIQGKS PYQLLSPILP
VLFKKMGRSL VEKKLGLQRI VQLVDYPAKT LLENFQRYVV PSALGQYKSD VITEVARIMS
GNDKSLVEEK KLKLLDRNSR QIFAVALVKH GFFSIETIQT LFLNTAPKFR KNYITLYLPD
YKTLAEVLKM SKQILTLDGQ ITETERCVLS SLRFLLITNF SKDKRRGTRF KNIEDWNEEM
EEQFQQKLEQ NVLGIFQVFS NDMHDSDGKT SYYEKLRVLN GISFLMKYAS KKSIISALAQ
LSICLQTGSE IPEIQHNTLE CWHLLIKLLN EEQITAIIND LFCLILQKWS TFSSSCKLEC
QAIFDTLLKD RQKLVLEGRP FILLAFLNNP EFQVLERHPT VARKVLKVIS TTNWLKVFTE
NLGSNNRYVI LQTLLELEKY FSTTIHRKHV DVVTKHDDSS HLSTLLGALL DSTYKFRNRD
LKICQIAASC ISLIGLLDVT KHALPRNTNL SEEICDFNNH SQTVKFLISI VNNILVPAFW
QSENPTKQLF VALVMQESLK YCGLSSVNWD INRPDDYPVE AKLWSRFNDI SKTTLFPLLS
SLYLAQSWKE YVPLSYPSFK VKDGYQVWIR NLTLDLLKIG TEEDHPLHVF SSLIREDDGT
LSNFLLPFIT MDIILRANKH NEYSKIIENL SIEFEFIFNF DLQQLNHFQI DSLKMAYNTI
FRVYEYCKKW VSSFKQDYQA ANGTYMIQED KVLQVLDRTE RFVNTIPSDT LAKKSLETDS
FERSALYLEQ SYREHGTSSL ASTDLLQCIQ NTYAEIGDVD AVGGVLKMFS TGNLTTKIEE
LQYSKNWKMA QDCFEALGDF KLSANSTTSS ELVKSSNMKM LKSMYSHQLY EELLMKVKVH
LPETKGFLVD NDGDLLNMGI EAVSQTGNIV ELTRWIERVE HIQMFNDPSL LLHYNIAKVL
QAVSRNQQQN VERYINKCFT LIGAQFTIPS TSTTLLKNRE VLQKLHALTD IKLLCSAHTQ
SEFSNASKAL DGRLSHVGSD FSPNHYLLSI RKTVEIISKN QHLQNDISNV YFQLSQLDRK
ENRLDLAAED LMNALKYNHH SAELEFAEIL WKQGEKDMAL KTVAEITKRF KDDPSTASSE
NQDFKEVLLK YTEWLDLSNS SVSEQIIKQY NELIRFDKNW DAPFYSMGLY YSKLLEKKKA
EGYVSDGSLE YRSITNFLTS FEKGSPNIRQ SLPKVVTLWL DTAKNDVNNS ISDVSNYSSR
ICNKIDTAVK NCGIHIWYTV LTQLLSRLMH PHTATIHTIV NILFHMTLEY PSVMLWYISI
LLNSESLERR NIGKQIVEAF QKKNPRTKLP GTAISLVQSL TRVCIKDVKN TASRSGRSID
SDFKFNLELA PNDMCVPVNI NLKKLLPSTA TSMNSDLFKS VMVSIARFSS QYMVFNSLKK
PKKLTVIGSD GNIYGIMCKK EDVRQDNQYM QFANTMSFLL SKDVESRKRN LGITTYGVLS
LREDCGLLEI VPNVVTLRSL LSMKYESMKI KYSLKSLQEK WQSIPSDQKL AFHKDCLKKF
PPVLYQWFLD NFPDPITWYN ARNGFVRSYS VMAMVGHILG LGDRHCENIL LDVLTGRVLH
VDFDCLFEKG KKLPVPEIVP FRLTQNITDA FGIIGTEGTF KKSSEVTLRV MRNNEIGLVN
IIETIMYDRK IDESIQNALK VLRDKIRGID ARDGLALSVS GQVEALTQES CSVENLSKMY
IGWLPFW


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